F-ATPases synthesize ATP from ADP and phosphate coupled with an electrochemical proton
gradient in bacterial or mitochondrial membranes and can hydrolyse ATP to form the gradient.
F-ATPases consist of a catalytic F1 and proton channel F0 formed from the a3b3gd3 and ab2c10
subunit complexes, respectively. The rotation of g3c10 couples catalyses and proton transport.
Consistent with the threefold symmetry of the a3b3 catalytic hexamer, 1208 stepped revolution has
been observed, each step being divided into two substeps. The ATP-dependent revolution exhibited
stochastic fluctuation and was driven by conformation transmission of the b subunit (phosphatebinding
P-loop/a-helix B/loop/b-sheet4). Recent results regarding mechanically driven ATP
synthesis finally proved the role of rotation in energy couplin